Search results for: Anti-ADAM-15, Cytoplasmic Domain produced in rabbit Antibody
#32068790 // To Up
Structural and functional comparison of fumarylacetoacetate domain containing protein 1 in human and mouse.FAH domain containing protein 1 (FAHD1) is a mammalian mitochondrial protein, displaying bifunctionality as acylpyruvate hydrolase (ApH) and oxaloacetate decarboxylase (ODx) activity. We report the crystal structure of mouse FAHD1 and structural mapping of the active site of mouse FAHD1. Despite high structural similarity with human FAHD1, a rabbit monoclonal antibody (RabMab) could be produced that is able to recognize mouse FAHD1, but not the human form, whereas a polyclonal antibody recognized both proteins. Epitope mapping in combination with our deposited crystal structures revealed that the epitope overlaps with a reported SIRT3 deacetylation site in mouse FAHD1.
Alexander K H Weiss, Andreas Naschberger, Elia Cappuccio, Christina Metzger, Lorenza Mottes, Max Holzknecht, Jill von Velsen, Matthew W Bowler, Bernhard Rupp, Pidder Jansen-DÃ¼rr
2298 related Products with: Structural and functional comparison of fumarylacetoacetate domain containing protein 1 in human and mouse.100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ul100ug Lyophilized100ug Lyophilized100uL100ug Lyophilized10mg100uL100ug Lyophilized
#32013223 2020/01/29 To Up
Immunogenicity of HIV-1 Vaccines Expressing Chimeric Envelope Glycoproteins on the Surface of Pr55 Gag Virus-Like Particles.The HIV-1 envelope glycoprotein (Env) is present on the surface of the virion at a very low density compared to most other enveloped viruses. Substitution of various parts of the stalk domain of Env (gp41) with the corresponding elements from other viral glycoproteins has been shown to increase Env spike density on the cell membrane and surface of virus-like particles (VLPs). In this study, chimeric Env antigens were generated by replacing the transmembrane and cytoplasmic domains of HIV-1 Env with the corresponding regions from the influenza H5 hemagglutinin (HA) (gp140HAtr) and by replacing the entire gp41 region of Env with the HA subunit of HA (gp120HA). Recombinant DNA and modified vaccinia Ankara (MVA) vaccines expressing HIV-1 subtype C mosaic Gag and gp150 Env or either of the chimeras were generated. Surprisingly, no significant differences were found in the levels of expression of gp150 Env or either of the chimeras on the surface of cells or on Gag VLPs. Differences were, however, observed in the binding of different monoclonal antibodies to the HIV-1 Env. Monoclonal antibodies, which recognized a V1 / V2 quaternary epitope at the tip of the native Env trimer, bound gp150 and gp140HAtr chimera but failed to bind to the gp120HA chimera. Autologous Tier 2 neutralizing antibodies (NAbs) were produced by rabbits inoculated with DNA and MVA vaccines expressing the gp140HAtr chimera or gp150 Env, but not those immunized with the gp120HA Env. These results showed that the addition of an HA stalk to HIV-1 gp120 did not improve immunogenicity, but rather that the full-length gp150 was required for optimal presentation of epitopes for the elicitation of a neutralizing antibody response to HIV-1.
Rosamund Chapman, Michiel van Diepen, Shireen Galant, Elizabeth Kruse, Emmanuel Margolin, Phindile Ximba, Tandile Hermanus, Penny Moore, Nicola Douglass, Anna-Lise Williamson, Edward Rybicki
1778 related Products with: Immunogenicity of HIV-1 Vaccines Expressing Chimeric Envelope Glycoproteins on the Surface of Pr55 Gag Virus-Like Particles.10001x107 IFU/ml x 200ul10001000 1000 10001000100ug Lyophilized100ug Lyophilized100ug Lyophilized100μg100ug
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#29708866 // To Up
The Characterization of Monoclonal Antibodies to Mouse TLT-1 Suggests That TLT-1 Plays a Role in Wound Healing.Platelets play a vital role in hemostasis and inflammation. The membrane receptor TREM-like transcript-1 (TLT-1) is involved in platelet aggregation, bleeding, and inflammation, and it is localized in the Î±-granules of platelets. Upon platelet activation, TLT-1 is released from Î±-granules both in its transmembrane form and as a soluble fragment (sTLT-1). Higher levels of sTLT-1 have been detected in the plasma of patients with acute inflammation or sepsis, suggesting an important role for TLT-1 during inflammation. However, the roles of TLT-1 in hemostasis and inflammation are not well understood. We are developing the mouse model of TLT-1 to mechanistically test clinical associations of TLT-1 in health and disease. To facilitate our studies, monoclonal murine TLT-1 (mTLT-1) antibodies were produced by the immunization of a rabbit using the negatively charged region of the mTLT-1 extracellular domain PPVPGPREGEEAEDEK. In the present study, we demonstrate that two selected clones, 4.6 and 4.8, are suitable for the detection of mTLT-1 by western blot, immunoprecipitation, immunofluorescent staining, flow cytometry and inhibit platelet aggregation in aggregometry assays. In addition, we found that the topical administration of clone 4.8 delayed the wound healing process in an experimental burn model. These results suggest that TLT-1 plays an important role in wound healing and because both clones specifically detect mTLT-1, they are suitable to further develop TLT-1 based models of inflammation and hemostasis in vivo.
Barbara Manfredi, Jessica Morales-OrtÃz, Lymarie M DÃaz-DÃaz, Liz Hernandez-Matias, Delmaliz Barreto-VÃ¡zquez, Javier MenÃ©ndez-PÃ©rez, J Alejandro RodrÃguez-Cordero, Juan C Villalobos-Santos, Edgardo Santiago-Rivera, Adriana Rivera-Dompenciel, Eunice L Lozada-Delgado, Madhavi Kuchibhotla, Kelvin Carrasquillo-CarriÃ³n, Abiel Roche-Lima, A Valance Washington
1360 related Products with: The Characterization of Monoclonal Antibodies to Mouse TLT-1 Suggests That TLT-1 Plays a Role in Wound Healing.100.00 ug100ug100 ug100ug100ul100ug100ug100ug Lyophilized100.00 ug100ug Lyophilized100ug100ug
#29113861 2017/11/04 To Up
Identification and characterization of myeloperoxidase in orange-spotted grouper (Epinephelus coioides).Cryptocaryon irritans is an important protozoan ciliate, which has led to heavy economic losses in marine aquaculture. Previous studies have indicated that C. irritans infection could induce the migration of neutrophils to infection sites. Myeloperoxidase (MPO) mainly exists in the cytoplasmic granules of the neutrophil and performs its function by a unique enzymatic capacity to produce hypohalous acid and other toxic oxidants. To determine the involvement of MPO and neutrophils against C. irritans infection in the host, we amplified MPO cDNA (EcMPO) from orange-spotted grouper (Epinephelus coioides). The open reading frame (ORF) of EcMPO encodes a putative polypeptide of 770 amino acids and has typical structural characteristics of mammalian MPO, including a signal peptide, a propeptide, a light chain, a heavy chain, and a peroxidase domain. Bioinformatics analysis has demonstrated that the most important functional sites in mammalian MPO were also conserved in grouper and other piscine MPO, implying the functional conservation of this protein during evolution. A rabbit anti-MPO recombinant protein polyclonal antibody was produced, which could recognize the native MPO protein. The expression of EcMPO was higher in the lympho-hematopoietic organs, such as head kidney, trunk kidney, spleen, but lower in muscle, heart, and brain. After infection with C. irritans, the EcMPO transcript was significantly up-regulated at specific time points in the infection sites (skin and gill) and systemic immune organs (head kidney and spleen); The number of EcMPO positive cells first increased and then decreased in the gill, but was still higher than the control after 7 days. These results demonstrated that EcMPO and its positive cells may be involved in anti-C. irritans infection in the grouper, which is attributed to the innate immune mechanisms of the host against parasite infection.
Hai-Qing Wang, Ling Zhou, Man Yang, Xiao-Chun Luo, Yan-Wei Li, Xue-Ming Dan
1399 related Products with: Identification and characterization of myeloperoxidase in orange-spotted grouper (Epinephelus coioides).100 mg5 mg1 kit1 mg500 mg500 mg100 mg100 ul 5 G1 Set100ug Lyophilized
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#25732411 2015/02/25 To Up
Characterisation of a Babesia orientalis apical membrane antigen, and comparison of its orthologues among selected apicomplexans.In the present study, we identified and characterised the complete coding sequence of Babesia orientalis apical membrane antigen 1 (designated Bo-ama1); it is 1803bp in length and encodes a polypeptide of 601 amino acids (aa). The Bo-ama-1 gene product (Bo-AMA1) is predicted to be 67kDa in size and contains a signal peptide. Mature Bo-AMA1 is predicted to have one transmembrane region and a short cytoplasmic tail (C-terminal domain). The extracellular part of Bo-AMA1 has three functional domains (DI, DII and DIII) with 14 conserved cysteine residues. A Bo-AMA1 fragment containing all three of these domains (designated Bo-AMA1-DI/II/III) was cloned into the plasmid vector pET-28a and expressed as a recombinant (His-fusion) protein of 53kDa. Antibodies in the serum from a B. orientalis-infected water buffalo specifically recognised this protein in immunoblotting analysis. Rabbit antibodies raised against the recombinant protein were able to detect native Bo-AMA1 (67kDa) from erythrocytes of B. orientalis-infected water buffalo. Bo-AMA1 is a new member of the AMA1 family and might be a good antigen for the specific detection of antibodies produced in B. orientalis infected cattle. This protein is likely to play critical roles during host cell adherence and invasion by B. orientalis, as the AMA1s reported in other organisms such as Plasmodium falciparum and Toxoplasma gondii. Further research is required to explore the biological functions of this protein and to determine whether its immunisation can induce protective effects in water buffalo against B. orientalis infection.
Lan He, Lizhe Fan, Jinfang Hu, Xiaoyan Miao, Yuan Huang, Yanqin Zhou, Min Hu, Junlong Zhao
1739 related Products with: Characterisation of a Babesia orientalis apical membrane antigen, and comparison of its orthologues among selected apicomplexans.100 25 ml Ready-to-use 0.1 ml1 mL 6 ml Ready-to-use 2 ml Ready-to-use 25 5 plate kit96T50ul200 100 µg
#24577000 2014/02/19 To Up
Dual localization of Mdj1 in pathogenic fungi varies with growth temperature.Paracoccidioides brasiliensis and P. lutzii are temperature-dependent dimorphic fungi that cause paracoccidioidomycosis (PCM). Previously, we characterized the PbMDJ1 gene. This gene encodes P. brasiliensis chaperone Mdj1, which in yeast is a mitochondrial member of the J-domain family, whose main function is to regulate cognate Hsp70 activities. We produced rabbit polyclonal antibody antirecombinant PbMdj1 (rPbMdj1), which labeled the protein not only in mitochondria but also at the cell wall of P. brasiliensis yeasts of isolate Pb18. Here we used anti-rPbMdj1 in confocal microscopy to localize Mdj1 in Pb18 and other fungal isolates grown at different temperatures. Dual intracellular and cell surface pattern were initially seen in yeast-phase P. brasiliensis Pb3, Pb18 (control), P. lutzii Pb01, and Histoplasma capsulatum. Pb18 and Aspergillus fumigatus hyphae as well as Pb3 pseudo hyphae formed at 36Â°C were labeled predominantly along the cell surface. Preferential surface localization was observed by 72 h of yeast-mycelium thermotransition. It was interesting to observe that anti-rPbMdj1 concentrated at the surface tip and branching points of A. fumigatus hyphae grown at 36Â°C, suggesting a role in growth, whereas at 23Â°C, anti-rPbMdj1 was distributed along the hyphal surface. In Pb3, Pb18, and Pb01 mitochondrial extracts, the antibodies revealed a specific 55-kDa band, which corresponds to the processed Mdj1 size. The presence of Mdj1 on the fungal cell wall suggests that this protein could also play a role in the interaction with the host.
Itala Bruna Z Dourado, Wagner L Batista, Larissa V G Longo, Renato A Mortara, Rosana Puccia
2113 related Products with: Dual localization of Mdj1 in pathogenic fungi varies with growth temperature.20 ul100.00 ug10ug20 ul10ug10ug100.00 ug50 ul20 ul100.00 ug50 ul
#22921497 2012/08/16 To Up
Leishmania (Viannia) braziliensis nucleoside triphosphate diphosphohydrolase (NTPDase 1): localization and in vitro inhibition of promastigotes growth by polyclonal antibodies.Nucleoside triphosphate diphosphohydrolase (NTPDase) activity was recently characterized in Leishmania (Viannia) braziliensis promastigotes (Lb), and an antigenic conserved domain (r82-121) from the specific NTPDase 1 isoform was identified. In this work, mouse polyclonal antibodies produced against two synthetic peptides derived from this domain (LbB1LJ, r82-103; LbB2LJ, r102-121) were used. The anti-LbB1LJ or anti-LbB2LJ antibodies were immobilized on protein A-sepharose and immunoprecipitated the NTPDase 1 of 48 kDa and depleted approximately 40% of the phosphohydrolytic activity from detergent-homogenized Lb preparation. Ultrastructural immunocytochemical microscopy identified the NTPDase 1 on the parasite surface and in its subcellular cytoplasmic vesicles, mitochondria, kinetoplast and nucleus. The ATPase and ADPase activities of detergent-homogenized Lb preparation were partially inhibited by anti-LbB1LJ antibody (43-79%), which was more effective than that inhibition (18-47%) by anti-LbB2LJ antibody. In addition, the immune serum anti-LbB1LJ (67%) or anti-LbB2LJ (33%) was cytotoxic, significantly reducing the promastigotes growth in vitro. The results appoint the conserved domain from the L. braziliensis NTPDase as an important target for inhibitor design and the potential application of these biomolecules in experimental protocols of disease control.
Gabriane Nascimento Porcino, Cristiane Carvalho-Campos, Ana Carolina Ribeiro Gomes Maia, Michelle Lima Detoni, Priscila Faria-Pinto, Elaine Soares Coimbra, Marcos JosÃ© Marques, Maria Aparecida Juliano, Luiz Juliano, Vanessa Ãlvaro Diniz, Suzana Corte-Real, Eveline Gomes Vasconcelos
1154 related Products with: Leishmania (Viannia) braziliensis nucleoside triphosphate diphosphohydrolase (NTPDase 1): localization and in vitro inhibition of promastigotes growth by polyclonal antibodies.100 μg100.00 ug100.00 ug4 Membranes/Box100.00 ug100.00 ug2 Pieces/Box100.00 ug100.00 ug100ug Lyophilized100ug Lyophilized100ug
#20693967 // To Up
Immunocytochemical study of Bcr and Bcr-Abl localization in K562 cells.To obtain polyclonal antibodies against recombinant proteins recognizing Bcr domain and fusion region of Bcr-Abl and analyze the patterns of intracellular distribution of Bcr and Bcr-Abl proteins in K562 cells of chronic myelogenous leukemia.
G D Telegeev, A N Dubrovska, V A Nadgorna, M V Dybkov, M P Zavelevich, S S Maliuta, D F Gluzman1x10e7 cells100 µg96 wells1 mg1x10e7 cells10 rxns-100 µg96 assays10 ug1.00 flask
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